Publications

1.             Ribeiro VC, Wirtz J, Leidecker O. The beauty of ADP-ribosylation: versatility in every link and organelle. BIOspektrum. 2025;31(3):258-61.

2.             Strachan J, Leidecker O, Spanos C, Le Coz C, Chapman E, Arsenijevic A, et al. SUMOylation regulates Lem2 function in centromere clustering and silencing. J Cell Sci. 2023;136(23).

3.             Bonfiglio JJ*, Leidecker O*, Dauben H*, Longarini EJ*, Colby T, San Segundo-Acosta P, et al. An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell. 2020;183(4):1086-102 e23.

4.             Fatima A, Irmak D, Noormohammadi A, Rinschen MM, Das A, Leidecker O, et al. The ubiquitin-conjugating enzyme UBE2K determines neurogenic potential through histone H3 in human embryonic stem cells. Commun Biol. 2020;3(1):262.

5.             Palazzo L*, Leidecker O*, Prokhorova E*, Dauben H, Matic I, Ahel I. Serine is the major residue for ADP-ribosylation upon DNA damage. Elife. 2018;7.

6.             Leidecker O*, Bonfiglio JJ*, Colby T, Zhang Q, Atanassov I, Zaja R, et al. Serine is a new target residue for endogenous ADP-ribosylation on histones. Nat Chem Biol. 2016;12(12):998-1000.

7.             Palazzo L, Thomas B, Jemth AS, Colby T, Leidecker O, Feijs KL, et al. Processing of protein ADP-ribosylation by Nudix hydrolases. Biochem J. 2015;468(2):293-301.

8.             Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, et al. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Mol Cell. 2015;59(2):309-20.